Abstract
1,2-Diacylglycerol kinase activity was measured in human erythrocyte membranes using an assay procedure in which the substrate was generated endogenuously, either by treatment with a bacterial phospholipase C or by incubation with Ca2+, which activates a membrane-bound polyphosphoinositide phosphodiesterase. The properties of 1,2-diacylglycerol kinase were broadly similar to those described previously, except that in the present work maximum activities were higher and there was evidence for a double pH optimum.
| Original language | English |
|---|---|
| Pages (from-to) | 669-672 |
| Number of pages | 4 |
| Journal | Biochemical Journal |
| Volume | 191 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1980 |
| Externally published | Yes |